ArticleMolecular and cellular biochemistry2001
Phosphorylation of the triadin cytoplasmic domain by CaM protein kinase in rabbit fast-twitch muscle sarcoplasmic reticulum.
Article in Molecular and cellular biochemistry, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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Who cites it
2 citing papers in PubMed, 11 citations in OpenAlex.
- Regulation and function of Ca2+-calmodulin-dependent protein kinase II of fast-twitch rat skeletal muscle.The Journal of physiology · 2007Article
- Calmodulin kinase modulates Ca2+ release in mouse skeletal muscle.The Journal of physiology · 2003Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Skeletal muscle triadin is a sarcoplasmic reticulum (SR) membrane protein that had been shown to interact structurally and functionally at the cytoplasmic domain (amino acid residues 1-47) with the ryanodine receptor (RyR1), and to undergo phosphorylation by endogenous calmodulin protein kinase (CaM K II) in isolated terminal cisternae from rabbit fast-twitch muscle. Here we show that triadin cytoplasmic domain expressed as glutathione-S-transferase fusion protein, is a substrate of the protein kinase. This finding is corroborated by identification of a specific consensus sequence in the deduced amino sequence between residue 34 and 37 of triadin. Confirming the regulatory features of CaM K II, we show the phosphorylation of triadin cytoplasmic segment by the kinase, when converted to the autonomous form. We propose that triadin modulates RyR1 in a phosphorylation-dependent manner.
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